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Protein

Acid-sensing ion channel 3

Gene

Asic3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei26Potassium ion selectivity and permeability1

GO - Molecular functioni

  • enterobactin transporter activity Source: Ensembl
  • ligand-gated sodium channel activity Source: MGI
  • PDZ domain binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Protein family/group databases

TCDBi1.A.6.1.2. the epithelial na(+) channel (enac) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid-sensing ion channel 3
Short name:
ASIC3
Alternative name(s):
Amiloride-sensitive cation channel 3
Dorsal root ASIC
Short name:
DRASIC
Gene namesi
Name:Asic3
Synonyms:Accn3, Drasic
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi708578. Asic3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Topological domaini41 – 435ExtracellularSequence analysisAdd BLAST395
Transmembranei436 – 456HelicalSequence analysisAdd BLAST21
Topological domaini457 – 533CytoplasmicSequence analysisAdd BLAST77

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20V → P: No effect on selectivity or channel function. 1 Publication1
Mutagenesisi21F → S: Loss of channel function. 1 Publication1
Mutagenesisi26T → K: Alters selectivity of the channel for sodium. No effect on channel function. 1 Publication1
Mutagenesisi40T → G: Loss of regulation by PKC through PRKCABP; when associated with G-523. 1 Publication1
Mutagenesisi523S → G: Loss of regulation by PKC through PRKCABP; when associated with G-40. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001813031 – 533Acid-sensing ion channel 3Add BLAST533

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40Phosphothreonine; by PKC1 Publication1
Disulfide bondi93 ↔ 187By similarity
Disulfide bondi165 ↔ 172By similarity
Glycosylationi176N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi283 ↔ 372By similarity
Disulfide bondi317 ↔ 368By similarity
Disulfide bondi321 ↔ 366By similarity
Disulfide bondi330 ↔ 352By similarity
Disulfide bondi332 ↔ 344By similarity
Glycosylationi400N-linked (GlcNAc...)Sequence analysis1
Modified residuei523Phosphoserine; by PKC1 Publication1

Post-translational modificationi

Phosphorylated by PKA (By similarity). Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric ASIC3/ACCN3 channel.By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO35240.
PRIDEiO35240.

PTM databases

iPTMnetiO35240.
PhosphoSitePlusiO35240.

Expressioni

Tissue specificityi

Expressed in sciatic nerve and dorsal root ganglion (at protein level). Expressed in sensory neurons of dorsal root ganglion. Expressed in Golgi interneurons in the granular layer. Also found in superior cervical ganglia, spinal chord and brain stem.4 Publications

Developmental stagei

Expression is first detected at E15.5. Strongly expressed perinatally.1 Publication

Inductioni

Transcriptionally regulated by the proinflamatory mediators nerve growth factor, serotonin, interleukin-1 and bradykinin. Up-regulation upon tissues inflammation is abolished by anti-inflammatory drugs.3 Publications

Gene expression databases

GenevisibleiO35240. RN.

Interactioni

Subunit structurei

Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with LIN7B, MAGI1 and GOPC (By similarity). Interacts with DLG4 and ASIC2. Interacts with STOM; this regulates channel activity.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
InadlQ63ZW7-32EBI-982374,EBI-8158524From a different organism.
Slc9a3r1Q9JJ195EBI-982374,EBI-982391
Slc9a3r2Q920G22EBI-982374,EBI-982439
StomP541163EBI-982374,EBI-8004826From a different organism.

GO - Molecular functioni

  • PDZ domain binding Source: RGD

Protein-protein interaction databases

DIPiDIP-35759N.
IntActiO35240. 4 interactors.
MINTiMINT-1777886.
STRINGi10116.ENSRNOP00000011300.

Chemistry databases

BindingDBiO35240.

Structurei

3D structure databases

ProteinModelPortaliO35240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi530 – 533PDZ-bindingBy similarity4

Domaini

The PDZ domain-binding motif is involved in interaction with LIN7A, GOPC and MAGI1/BAIAP1.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
GeneTreeiENSGT00760000119120.
HOGENOMiHOG000247010.
HOVERGENiHBG004150.
InParanoidiO35240.
KOiK04830.
OMAiTCPNPCA.
OrthoDBiEOG091G053J.
PhylomeDBiO35240.
TreeFamiTF330663.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 1 hit.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPRSGLEEA QRRQASDIRV FASSCTMHGL GHIFGPGGLT LRRGLWATAV
60 70 80 90 100
LLSLAAFLYQ VAERVRYYGE FHHKTTLDER ESHQLTFPAV TLCNINPLRR
110 120 130 140 150
SRLTPNDLHW AGTALLGLDP AEHAAYLRAL GQPPAPPGFM PSPTFDMAQL
160 170 180 190 200
YARAGHSLED MLLDCRYRGQ PCGPENFTVI FTRMGQCYTF NSGAHGAELL
210 220 230 240 250
TTPKGGAGNG LEIMLDVQQE EYLPIWKDME ETPFEVGIRV QIHSQDEPPA
260 270 280 290 300
IDQLGFGAAP GHQTFVSCQQ QQLSFLPPPW GDCNTASLDP DDFDPEPSDP
310 320 330 340 350
LGSPRPRPSP PYSLIGCRLA CESRYVARKC GCRMMHMPGN SPVCSPQQYK
360 370 380 390 400
DCASPALDAM LRKDTCVCPN PCATTRYAKE LSMVRIPSRA SARYLARKYN
410 420 430 440 450
RSESYITENV LVLDIFFEAL NYEAVEQKAA YEVSELLGDI GGQMGLFIGA
460 470 480 490 500
SLLTILEILD YLCEVFQDRV LGYFWNRRSA QKRSGNTLLQ EELNGHRTHV
510 520 530
PHLSLGPRPP TTPCAVTKTL SASHRTCYLV TRL
Length:533
Mass (Da):59,227
Last modified:January 1, 1998 - v1
Checksum:i294B57322C74B3DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013598 mRNA. Translation: AAB69328.1.
RefSeqiNP_775158.1. NM_173135.1.
UniGeneiRn.24225.

Genome annotation databases

EnsembliENSRNOT00000011300; ENSRNOP00000011300; ENSRNOG00000008380.
GeneIDi286920.
KEGGirno:286920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013598 mRNA. Translation: AAB69328.1.
RefSeqiNP_775158.1. NM_173135.1.
UniGeneiRn.24225.

3D structure databases

ProteinModelPortaliO35240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35759N.
IntActiO35240. 4 interactors.
MINTiMINT-1777886.
STRINGi10116.ENSRNOP00000011300.

Chemistry databases

BindingDBiO35240.
ChEMBLiCHEMBL5757.

Protein family/group databases

TCDBi1.A.6.1.2. the epithelial na(+) channel (enac) family.

PTM databases

iPTMnetiO35240.
PhosphoSitePlusiO35240.

Proteomic databases

PaxDbiO35240.
PRIDEiO35240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011300; ENSRNOP00000011300; ENSRNOG00000008380.
GeneIDi286920.
KEGGirno:286920.

Organism-specific databases

CTDi9311.
RGDi708578. Asic3.

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
GeneTreeiENSGT00760000119120.
HOGENOMiHOG000247010.
HOVERGENiHBG004150.
InParanoidiO35240.
KOiK04830.
OMAiTCPNPCA.
OrthoDBiEOG091G053J.
PhylomeDBiO35240.
TreeFamiTF330663.

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Miscellaneous databases

PROiO35240.

Gene expression databases

GenevisibleiO35240. RN.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 1 hit.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiASIC3_RAT
AccessioniPrimary (citable) accession number: O35240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Potentiated by FMRFamide-related neuropeptides (By similarity). Sensitized and potentiated by NPFF and NPSF. Regulated by lactate and Ca2+. Specifically inhibited by APETx2, a sea anemone toxin. Inhibited by anti-inflammatory drugs like salicylic acid.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.